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Journal of Virology, September 2001, p. 7872-7874, Vol. 75, No. 17
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.17.7872-7874.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Copper Binding to the PrP Isoforms: a Putative Marker of Their Conformation and Function

Yuval Shaked, Hana Rosenmann, Nuha Hijazi, Michele Halimi, and Ruth Gabizon*

Department of Neurology, The Agnes Ginges Center for Human Neurogenetics, Hadassah University Hospital, Jerusalem, Israel

Received 25 January 2001/Accepted 18 May 2001

We show here that PrPC, the normal isoform of the prion protein (PrPSc), could be retained by a Cu2+-loaded resin through two different binding sites. Contrarily, PrPSc was not retained at all by such resin. This constitutes a new prion-specific property of PrPSc, which in addition to protease resistance and beta -sheet content, may result from its aberrant conformation.

* Corresponding author. Mailing address: Department of Neurology, Hadassah University Hospital, Jerusalem, Israel 91120. Phone: 972-2-6777858. Fax: 972-2-6429441. E-mail: gabizonr{at}hadassah.org.il.

Journal of Virology, September 2001, p. 7872-7874, Vol. 75, No. 17
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.17.7872-7874.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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